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Protein

Regulator of microtubule dynamics protein 3

Gene

Rmdn3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cellular calcium homeostasis regulation (By similarity). May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of microtubule dynamics protein 3
Short name:
RMD-3
Short name:
mRMD-3
Alternative name(s):
Protein FAM82A2
Protein FAM82C
Gene namesi
Name:Rmdn3
Synonyms:Fam82a2, Fam82c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1915059. Rmdn3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3523HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Microtubule, Mitochondrion, Mitochondrion outer membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Regulator of microtubule dynamics protein 3PRO_0000287511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei57 – 571PhosphoserineCombined sources
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei233 – 2331PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UJU9.
MaxQBiQ3UJU9.
PaxDbiQ3UJU9.
PRIDEiQ3UJU9.

PTM databases

iPTMnetiQ3UJU9.
PhosphoSiteiQ3UJU9.

Expressioni

Gene expression databases

BgeeiQ3UJU9.
CleanExiMM_1200015F23RIK.
ExpressionAtlasiQ3UJU9. baseline and differential.
GenevisibleiQ3UJU9. MM.

Interactioni

Subunit structurei

Interacts with PTPN2. Interacts with microtubules. Interacts with VAPB.By similarity

Protein-protein interaction databases

BioGridi212454. 77 interactions.
IntActiQ3UJU9. 78 interactions.
MINTiMINT-1839701.
STRINGi10090.ENSMUSP00000092283.

Structurei

3D structure databases

ProteinModelPortaliQ3UJU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili91 – 12535Sequence analysisAdd
BLAST

Domaini

The transmembrane region is required for mitochondrial localization.By similarity

Sequence similaritiesi

Belongs to the RMDN family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFRV. Eukaryota.
ENOG41101S6. LUCA.
GeneTreeiENSGT00530000063162.
HOGENOMiHOG000015374.
HOVERGENiHBG072518.
InParanoidiQ3UJU9.
OMAiEVRSHME.
OrthoDBiEOG7BP834.
PhylomeDBiQ3UJU9.
TreeFamiTF315854.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR011990. TPR-like_helical_dom.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3UJU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLGALGGS RAGLGLLLGT AAGLGFLCVL YSQRWKRTQR HGRSHSLPNS
60 70 80 90 100
LDYAQASERG RQVTQFRAIP GEAGDAAILP SLSQEGQEKV LDRLDFVLTS
110 120 130 140 150
LMALRREVEE LQRSLQGLAG EIVGEVRSHI EENQRVARRR RFPFARERSD
160 170 180 190 200
STGSSSVYFT ASSGAALTDA ESEGGYTTAN AESDYERDSD KESGDAEDEV
210 220 230 240 250
SCETVRMGRK DSLDLDVEAA SSPAAAALEE DDSSGREDVQ LVLLQADELH
260 270 280 290 300
QGSKQDKREG FQLLLNNKLA YGSRQDFLWR LARAYSDMSD LTEEESGKKS
310 320 330 340 350
YALNGKEEAE AALKKGDESA ACHLWYAVLC GQLAEHEGIS KRIQSGFSFK
360 370 380 390 400
EHVDKAIELQ PEDPRGHFLL GRWCYQVSHL NWLEKKTATA LFESPLSATV
410 420 430 440 450
QDALQSFLKA EELQPGFSKA GRVYISKCYR ELGKNSEARK WMKLAQELPD
460 470
VTNEDSAFQK DLEELEVILG
Length:470
Mass (Da):52,029
Last modified:May 15, 2007 - v2
Checksum:iBA82C57843985A1B
GO

Sequence cautioni

The sequence AAH55754.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH61186.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence FAA00420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101K → R in BAE31902 (PubMed:16141072).Curated
Sequence conflicti210 – 2101K → R in BAE31937 (PubMed:16141072).Curated
Sequence conflicti224 – 2241A → S in AAH61186 (PubMed:15489334).Curated
Sequence conflicti254 – 2541K → E in BAE27056 (PubMed:16141072).Curated
Sequence conflicti254 – 2541K → E in AAH61186 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146299 mRNA. Translation: BAE27056.1.
AK151090 mRNA. Translation: BAE30103.1.
AK153369 mRNA. Translation: BAE31937.1.
AK153322 mRNA. Translation: BAE31902.1.
AL772264 Genomic DNA. Translation: CAM45949.1.
BC055754 mRNA. Translation: AAH55754.1. Different initiation.
BC061186 mRNA. Translation: AAH61186.1. Sequence problems.
BR000695 mRNA. Translation: FAA00420.1. Different initiation.
CCDSiCCDS16591.1.
RefSeqiNP_001028308.1. NM_001033136.3.
UniGeneiMm.475909.

Genome annotation databases

EnsembliENSMUST00000094695; ENSMUSP00000092283; ENSMUSG00000070730.
GeneIDi67809.
KEGGimmu:67809.
UCSCiuc008lte.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146299 mRNA. Translation: BAE27056.1.
AK151090 mRNA. Translation: BAE30103.1.
AK153369 mRNA. Translation: BAE31937.1.
AK153322 mRNA. Translation: BAE31902.1.
AL772264 Genomic DNA. Translation: CAM45949.1.
BC055754 mRNA. Translation: AAH55754.1. Different initiation.
BC061186 mRNA. Translation: AAH61186.1. Sequence problems.
BR000695 mRNA. Translation: FAA00420.1. Different initiation.
CCDSiCCDS16591.1.
RefSeqiNP_001028308.1. NM_001033136.3.
UniGeneiMm.475909.

3D structure databases

ProteinModelPortaliQ3UJU9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212454. 77 interactions.
IntActiQ3UJU9. 78 interactions.
MINTiMINT-1839701.
STRINGi10090.ENSMUSP00000092283.

PTM databases

iPTMnetiQ3UJU9.
PhosphoSiteiQ3UJU9.

Proteomic databases

EPDiQ3UJU9.
MaxQBiQ3UJU9.
PaxDbiQ3UJU9.
PRIDEiQ3UJU9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094695; ENSMUSP00000092283; ENSMUSG00000070730.
GeneIDi67809.
KEGGimmu:67809.
UCSCiuc008lte.2. mouse.

Organism-specific databases

CTDi55177.
MGIiMGI:1915059. Rmdn3.

Phylogenomic databases

eggNOGiENOG410IFRV. Eukaryota.
ENOG41101S6. LUCA.
GeneTreeiENSGT00530000063162.
HOGENOMiHOG000015374.
HOVERGENiHBG072518.
InParanoidiQ3UJU9.
OMAiEVRSHME.
OrthoDBiEOG7BP834.
PhylomeDBiQ3UJU9.
TreeFamiTF315854.

Miscellaneous databases

PROiQ3UJU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UJU9.
CleanExiMM_1200015F23RIK.
ExpressionAtlasiQ3UJU9. baseline and differential.
GenevisibleiQ3UJU9. MM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR011990. TPR-like_helical_dom.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Bone marrow.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Testis.
  4. "RMD-1, a novel microtubule-associated protein, functions in chromosome segregation in Caenorhabditis elegans."
    Oishi K., Okano H., Sawa H.
    J. Cell Biol. 179:1149-1162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRMD3_MOUSE
AccessioniPrimary (citable) accession number: Q3UJU9
Secondary accession number(s): A9UN03
, Q3U5Y8, Q3UB61, Q6P8M2, Q7TNF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: June 8, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.